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(Reference retrieved automatically from Google Scholar through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

The Human Nucleolar Protein FTSJ3 Associates with NIP7 and Functions in Pre-rRNA Processing

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Author(s):
Morello, Luis G. [1, 2, 3] ; Coltri, Patricia P. [4] ; Quaresma, Alexandre J. C. [5, 6] ; Simabuco, Fernando M. [1] ; Silva, Tereza C. L. [1] ; Singh, Guramrit [2, 3] ; Nickerson, Jeffrey A. [5, 6] ; Oliveira, Carla C. [4] ; Moore, Melissa J. [2, 3] ; Zanchin, Nilson I. T. [7]
Total Authors: 10
Affiliation:
[1] Ctr Nacl Pesquisa Energia & Mat, Lab Nacl Biociencias, Sao Paulo - Brazil
[2] Univ Massachusetts, Sch Med, Dept Biochem & Mol Pharmacol, Worcester, MA - USA
[3] Univ Massachusetts, Sch Med, Howard Hughes Med Inst, Worcester, MA 01605 - USA
[4] Univ Sao Paulo, Dept Biochem, Sao Paulo - Brazil
[5] Univ Massachusetts, Sch Med, Dept Cell Biol, Worcester, MA 01655 - USA
[6] Univ Massachusetts, Sch Med, Ctr Canc, Worcester, MA - USA
[7] Fundacao Oswaldo Cruz, Inst Carlos Chagas, Curitiba, Parana - Brazil
Total Affiliations: 7
Document type: Journal article
Source: PLoS One; v. 6, n. 12, p. e29174, 2011.
Web of Science Citations: 13
Abstract

NIP7 is one of the many trans-acting factors required for eukaryotic ribosome biogenesis, which interacts with nascent preribosomal particles and dissociates as they complete maturation and are exported to the cytoplasm. By using conditional knockdown, we have shown previously that yeast Nip7p is required primarily for 60S subunit synthesis while human NIP7 is involved in the biogenesis of 40S subunit. This raised the possibility that human NIP7 interacts with a different set of proteins as compared to the yeast protein. By using the yeast two-hybrid system we identified FTSJ3, a putative ortholog of yeast Spb1p, as a human NIP7-interacting protein. A functional association between NIP7 and FTSJ3 is further supported by colocalization and coimmunoprecipitation analyses. Conditional knockdown revealed that depletion of FTSJ3 affects cell proliferation and causes pre-rRNA processing defects. The major pre-rRNA processing defect involves accumulation of the 34S pre-rRNA encompassing from site A' to site 2b. Accumulation of this pre-rRNA indicates that processing of sites A0, 1 and 2 are slower in cells depleted of FTSJ3 and implicates FTSJ3 in the pathway leading to 18S rRNA maturation as observed previously for NIP7. The results presented in this work indicate a close functional interaction between NIP7 and FTSJ3 during pre-rRNA processing and show that FTSJ3 participates in ribosome synthesis in human cells. (AU)